The Enzyme Database

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Accepted name: formylmethanofuran dehydrogenase
Reaction: formylmethanofuran + H2O + acceptor = CO2 + methanofuran + reduced acceptor
For diagram of methane biosynthesis, click here
Glossary: methanofuran = 4-[4-(2-{[(4R*,5S*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furfurylamine
Other name(s): formylmethanofuran:(acceptor) oxidoreductase
Systematic name: formylmethanofuran:acceptor oxidoreductase
Comments: A molybdoprotein containing a pterin cofactor. Tungstate can substitute for molybdate. The enzyme catalyses a reversible reaction in methanogenic bacteria, and is involved in methanogenesis from CO2 as well as the oxidation of methyl-coenzyme M to CO2. Methylviologen can act as acceptor. Also oxidizes N-furfurylformamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 119940-12-4
1.  Karrasch, M., Börner, G., Enssle, M. and Thauer, R.K. The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor. Eur. J. Biochem. 194 (1990) 367–372. [PMID: 2125267]
2.  Bertram, P.A., Schmitz, R.A., Linder, D. and Thauer, R.K. Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase. Arch. Microbiol. 161 (1994) 220–228. [PMID: 8161283]
3.  Bertram, P.A., Karrasch, M., Schmitz, R.A., Bocher, R., Albracht, S.P. and Thauer, R.K. Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. Eur. J. Biochem. 220 (1994) 477–484. [PMID: 8125106]
4.  Vorholt, J.A. and Thauer, R.K. The active species of ’CO2’ utilized by formylmethanofuran dehydrogenase from methanogenic Archaea. Eur. J. Biochem. 248 (1997) 919–924. [PMID: 9342247]
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